Does anyone have a good reference (beyond the original Crick & Magdoff
work) for the magnitude of non-isomorphism typically observed in protein
crystals? For example, two crystals from the same drop usually yield
scaled intensities that are within ~10% of each other, but cryo-cooling
usually changes F by 10-20%. At least, that has always been my
"impression", but now I find myself in need of a reference for this.
Surely someone has done some kind of survey of R-iso between cryo and RT
data sets?
-James Holton
MAD Scientist
|